Immobilization of Alpha-amylase and glucoamylase to sepharose - 4B

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Coupling of glycosaminoglycans to agarose beads (sepharose 4B).

1. Heparin, heparan sulphate, chondroitin sulphate and dermatan sulphate were covalently attached to beads of agarose activated by cyanogen bromide. The bond is probably mediated by the amino group of a serine or peptide residue at the reducing end of the polysaccharide chain. 2. The uptake of glycosaminoglycan during the coupling procedure is about 0.9mg/ml of wet gel. However, direct analysis...

متن کامل

Textural and Structural Characterizations of Mesoporous Chitosan Beads for Immobilization of Alpha-Amylase: Diffusivity and Sustainability of Biocatalyst

In the present study, textural and structural characterizations of chitosan bead for immobilization of alpha amylase were studied in detail by N2 adsorption–desorption, Microspore Analysis (MP), Barrett–Joyner–Halenda (BJH) plots and Field Emission Scanning Electron Microscope (FESEM) observations. Pore structure observation revealed chemical activation of chitosan bead by glutaralde...

متن کامل

Immobilization of Glucoamylase on Macroporous Spheres

Glucoamylase was covalently immobilized through the spacer-arm of the poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) spheres by using a glutaraldehyde as a coupling agent. The influence of the enzyme load, applied to the support on immobilization, yield and specific activity, has been determined. Obtained specific activity was 700 U/g with immobilization yield of 35 %. The Km val...

متن کامل

Isolation of rat transferrin using CNBr-activated sepharose 4B.

1. The isolation of transferrin from rat serum by means of affinity chromatography on CNBr-activated Sepharose 4 B is described. -2. Subfractionation by isoelectric focusing yielded two transferrin fractions with identical biological behaviour but with small differences in isoelectric point (6.0 and 5.8) and sialic acid contents.

متن کامل

Human amylase isoenzymes separated on concanavalin A--Sepharose.

Human salivary amylase and pancreatic amylase were purified and characterized. These amylases gave two bands and one band, respectively, each staining for both protein and sugar, after electrophoresis on sodium dodecyl sulfate--polyacrylamide gel. The relative molecular mass (Mr) or pancreatic amylase was calculated to be 60 000; for the two components (A and B) of salivary amylase the Mr were ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Journal of the National Science Foundation of Sri Lanka

سال: 1987

ISSN: 2362-0161,1391-4588

DOI: 10.4038/jnsfsr.v15i2.8296